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Information on EC 4.2.3.119 - (-)-alpha-pinene synthase and Organism(s) Abies grandis and UniProt Accession Q9M7D0
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4.2.3.119 (-)-alpha-pinene synthaseIUBMB Comments
Cyclase II of Salvia officinalis (sage) gives about equal parts (-)-alpha-pinene, (-)-beta-pinene and (-)-camphene, plus traces of other monoterpenoids. (3S)-Linalyl diphosphate can also be used by the enzyme in preference to (3R)-linalyl diphosphate. The 4-pro-S-hydrogen of geranyl diphosphate is lost. Requires Mg2+ (preferred to Mn2+) [1-6]. The enzyme from Abies grandis (grand fir) gives roughly equal parts (-)-alpha-pinene and (-)-beta-pinene. However the clone ag11 gave 35% (-)-limonene, 24% (-)-alpha-pinene and 20% (-)-beta-phellandrene. It requires Mn2+ and K+ (Mg2+ is ineffective) [7-10]. Synthase I from Pinus taeda (loblolly pine) produces (-)-alpha-pinene with traces of (-)-beta-pinene and requires Mn2+ (preferred to Mg2+) [11,12]. The enzyme from Picea sitchensis (Sika spruce) forms 70% (-)-alpha-pinene and 30% (-)-beta-pinene . The recombinant PmeTPS1 enzyme from Pseudotsuga menziesii (Douglas fir) gave roughly equal proportions of (-)-alpha-pinene and (-)-camphene plus traces of other monoterpenoids . See also EC 4.2.3.120, (-)-beta-pinene synthase; EC 4.2.3.117, (-)-camphene synthase; EC 4.2.3.16, (-)-limonene synthase; and EC 4.2.3.52, (-)-beta-phellandrene synthase.
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The taxonomic range for the selected organisms is: Abies grandis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
mono-tps, plpin, avtps1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(-)-alpha-pinene cyclase
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-
-
-
(-)-alpha-pinene/(-)-camphene synthase
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
geranyl-diphosphate diphosphate-lyase [cyclizing, (-)-alpha-pinene-forming]
Cyclase II of Salvia officinalis (sage) gives about equal parts (-)-alpha-pinene, (-)-beta-pinene and (-)-camphene, plus traces of other monoterpenoids. (3S)-Linalyl diphosphate can also be used by the enzyme in preference to (3R)-linalyl diphosphate. The 4-pro-S-hydrogen of geranyl diphosphate is lost. Requires Mg2+ (preferred to Mn2+) [1-6]. The enzyme from Abies grandis (grand fir) gives roughly equal parts (-)-alpha-pinene and (-)-beta-pinene. However the clone ag11 gave 35% (-)-limonene, 24% (-)-alpha-pinene and 20% (-)-beta-phellandrene. It requires Mn2+ and K+ (Mg2+ is ineffective) [7-10]. Synthase I from Pinus taeda (loblolly pine) produces (-)-alpha-pinene with traces of (-)-beta-pinene and requires Mn2+ (preferred to Mg2+) [11,12]. The enzyme from Picea sitchensis (Sika spruce) forms 70% (-)-alpha-pinene and 30% (-)-beta-pinene [13]. The recombinant PmeTPS1 enzyme from Pseudotsuga menziesii (Douglas fir) gave roughly equal proportions of (-)-alpha-pinene and (-)-camphene plus traces of other monoterpenoids [14]. See also EC 4.2.3.120, (-)-beta-pinene synthase; EC 4.2.3.117, (-)-camphene synthase; EC 4.2.3.16, (-)-limonene synthase; and EC 4.2.3.52, (-)-beta-phellandrene synthase.
CAS REGISTRY NUMBER
COMMENTARY
110637-20-2
for both EC 4.2.3.119 and 4.2.3.120
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
42% terpinolene, 18% (-)-alpha-pinene, 11% (-)-limonene, 10% (-)-beta-pinene plus several minor products
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?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
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-
about 40% (-)-alpha-pinene and 60% (-)-beta-pinene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
products are (-)-alpha-pinene and (-)-beta pinene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
-
products are 20% (-)-alpha-pinene, 6% (-)-beta-pinene, 26% (-)-limonene, 37% (-)-9-beta-phellandrene, and about 11% other monoterpenes
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
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products are 29% (-)-alpha-pinene, 63% (-)-beta-pinene, 1.8% myrcene, 3.6% limonene
-
?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
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-
products are 31.9% (-)-alpha-pinene and 63.9% (-)-beta-pinene, plus 4.2% myrcene
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?
geranyl diphosphate
(-)-alpha-pinene + diphosphate
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products are 54% (-)-(1S,4R)-camphene, followed by 32% (-)-(1S,5S)-alpha-pinene and 7% (-)-(4S)-limonene. (+)-alpha-pinene is produced to about 5% of (-)-alpha-pinene
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?
additional information
?
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entire product set is derived in stereochemically consistent fashion via (-)-3S-linalyl diphosphate as intermediate
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-
?
additional information
?
-
entire product set is derived in stereochemically consistent fashion via (-)-3S-linalyl diphosphate as intermediate
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.006
geranyl diphosphate
-
pH 7.8, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0019
4-hydroxymercuribenzoate
Abies grandis
-
pH 7.8, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
62000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
sequence contains a putative plastid targeting signal
proteolytic modification
proteolytic modification
sequence contains a putative N-terminal plastid targeting signal
proteolytic modification
sequence contains a putative N-terminal targeting peptide
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
modeling of amino acid sequence onto the crystal structures of tobacco 5-epi-aristolochene synthase and bornyl diphosphate synthase and comparison with (-)-camphene synthase
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C372S
replacement with corresponding residue of (-)-camphene synthase, 97% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant
C372S/C480S
replacement with corresponding residue of (-)-camphene synthase, 72% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
C372S/F597W
replacement with corresponding residue of (-)-camphene synthase, 100% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
C372S/F597W/S485C/F597W
replacement with corresponding residue of (-)-camphene synthase, 99% of wild-type activity. Mutant produces about 80%(-)-alpha-pinene and 10% (-)-beta-pinene
C372S/S485C
replacement with corresponding residue of (-)-camphene synthase, 92% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
C480S
replacement with corresponding residue of (-)-camphene synthase, 97% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant
C480S/F597W
replacement with corresponding residue of (-)-camphene synthase, 7% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
C480S/S485C
replacement with corresponding residue of (-)-camphene synthase, 70% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
F597W
replacement with corresponding residue of (-)-camphene synthase, 73% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant
S485C
replacement with corresponding residue of (-)-camphene synthase, 100% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant
S485C/F597W
replacement with corresponding residue of (-)-camphene synthase, 68% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
additional information
additional information
replacement of selected amino acid residues in (-)-pinene synthase with the corresponding residues from (-)-camphene synthase in an effort to identify the amino acids responsible for the catalytic diVerences. The approach produces an enzyme in which more than half of the product is channeled through an alternative pathway. Several (-)-pinene synthase to (-)-camphene synthase amino acid substitutions are necessary before catalysis is significantly altered
additional information
to elucidate critical amino acids involved in determining monoterpene product distribution, a combination of domain swapping and reciprocal site-directed mutagenesis was carried out between (-)-(4S)-limonene synthase LS and (-)-(4S)-limonene/(-)-(1S, 5S)-alpha-pinene synthase LPS. Amino acids in the predicted D through F helix regions are critical for product determination. Chimera consisting of N-terminal 218 residues of LS plus corresponding C-terminus of LPS produces 20.7% alpha-pinene, 11.2% sabinene, 7.1% beta-pinene, 25.6% limonene, 35.4% beta-phellandrene, with 42.8% relative activity. Chimera consisting of N-terminal 518 residues of LS plus corresponding C-terminus of LPS produces 6.4% alpha-pinene, 1.5% sabinene, 11% beta-pinene, 64.1% limonene, 17% beta-phellandrene, with 101% relative activity. Chimera consisting of N-terminal 442 residues of LPS plus corresponding C-terminus of LS produces 11% alpha-pinene, 1.4% sabinene, 6.3% beta-pinene, 47.9% limonene, 33.3% beta-phellandrene, with 41.7% relative activity
additional information
-
to elucidate critical amino acids involved in determining monoterpene product distribution, a combination of domain swapping and reciprocal site-directed mutagenesis was carried out between (-)-(4S)-limonene synthase LS and (-)-(4S)-limonene/(-)-(1S, 5S)-alpha-pinene synthase LPS. Amino acids in the predicted D through F helix regions are critical for product determination. Chimera consisting of N-terminal 218 residues of LS plus corresponding C-terminus of LPS produces 20.7% alpha-pinene, 11.2% sabinene, 7.1% beta-pinene, 25.6% limonene, 35.4% beta-phellandrene, with 42.8% relative activity. Chimera consisting of N-terminal 518 residues of LS plus corresponding C-terminus of LPS produces 6.4% alpha-pinene, 1.5% sabinene, 11% beta-pinene, 64.1% limonene, 17% beta-phellandrene, with 101% relative activity. Chimera consisting of N-terminal 442 residues of LPS plus corresponding C-terminus of LS produces 11% alpha-pinene, 1.4% sabinene, 6.3% beta-pinene, 47.9% limonene, 33.3% beta-phellandrene, with 41.7% relative activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme, stable at 4°C, in 50 mM Hepes, pH 7.8, for at least 3 weeks, at -20°C, stable for sevceral months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bohlmann, J.; Steele C.L.; Croteau, R.
Monoterpene synthases from grand fir (Abies grandis): cDNA isolation, characterization, and functional expression of myrcene synthase, (-)-(4S)-limonene synthase, and (-)-(1S,5S)-pinene synthase
J. Biol. Chem.
272
21784-21792
1997
Abies grandis (O24475)
Gijzen, M.; Lewinsohn, E.; Croteau, R
Characterization of the constitutive and wound-inducible monoterpene cyclases of grand fir (Abies grandis)
Arch. Biochem. Biophys.
289
267-273
1991
Abies grandis
Lewinsohn, E.; Gijzen, M.; Croteau, R.
Wound-inducible pinene cyclase from grand fir: Purification, characterization, and renaturation after SDS-PAGE
Arch. Biochem. Biophys.
293
167-173
1992
Abies grandis
Katoh S.;Hyatt D.;Croteau R.
Altering product outcome in Abies grandis (-)-limonene synthase and (-)-limonene/(-)-alpha-pinene synthase by domain swapping and directed mutagenesis
Arch. Biochem. Biophys.
425
65-76
2004
Abies grandis (Q9M7C9), Abies grandis
Hyat, D.C.; Croteau, R.
Mutational analysis of a monoterpene synthase reaction: altered catalysis through directed mutagenesis of (-)-pinene synthase from Abies grandis
Arch. Biochem. Biophys.
439
222-233
2005
Abies grandis (O24475)
Bohlmann, J.; Phillips, M.; Ramachandiran, V.; Katoh, S.; Croteau, R.
cDNA cloning, characterization, and functional expression of four new monoterpene synthase members of the Tpsd gene family from grand fir (Abies grandis)
Arch. Biochem. Biophys.
368
232-243
1999
Abies grandis (Q948Z0), Abies grandis (Q9M7D0)
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